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Molecular sensitised probe for amino acid recognition within peptide sequences

Xu Wu, Bogdana Borca, Suman Sen, Sebastian Koslowski, Sabine Abb, Daniel Pablo Rosenblatt, Aurelio Gallardo, Jesús I. Mendieta-Moreno, Matyas Nachtigall, Pavel Jelinek (), Stephan Rauschenbach (), Klaus Kern and Uta Schlickum ()
Additional contact information
Xu Wu: Max Planck Institute for Solid State Research
Bogdana Borca: Technische Universität Braunschweig
Suman Sen: Max Planck Institute for Solid State Research
Sebastian Koslowski: Max Planck Institute for Solid State Research
Sabine Abb: Max Planck Institute for Solid State Research
Daniel Pablo Rosenblatt: Max Planck Institute for Solid State Research
Aurelio Gallardo: Institute of Physics of the Czech Academy of Science
Jesús I. Mendieta-Moreno: Institute of Physics of the Czech Academy of Science
Matyas Nachtigall: Institute of Physics of the Czech Academy of Science
Pavel Jelinek: Institute of Physics of the Czech Academy of Science
Stephan Rauschenbach: Max Planck Institute for Solid State Research
Klaus Kern: Max Planck Institute for Solid State Research
Uta Schlickum: Max Planck Institute for Solid State Research

Nature Communications, 2023, vol. 14, issue 1, 1-8

Abstract: Abstract The combination of low-temperature scanning tunnelling microscopy with a mass-selective electro-spray ion-beam deposition established the investigation of large biomolecules at nanometer and sub-nanometer scale. Due to complex architecture and conformational freedom, however, the chemical identification of building blocks of these biopolymers often relies on the presence of markers, extensive simulations, or is not possible at all. Here, we present a molecular probe-sensitisation approach addressing the identification of a specific amino acid within different peptides. A selective intermolecular interaction between the sensitiser attached at the tip-apex and the target amino acid on the surface induces an enhanced tunnelling conductance of one specific spectral feature, which can be mapped in spectroscopic imaging. Density functional theory calculations suggest a mechanism that relies on conformational changes of the sensitiser that are accompanied by local charge redistributions in the tunnelling junction, which, in turn, lower the tunnelling barrier at that specific part of the peptide.

Date: 2023
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43844-5

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DOI: 10.1038/s41467-023-43844-5

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